Characterization of a novel trans-sialidase of Trypanosoma brucei procyclic trypomastigotes and identification of procyclin as the main sialic acid acceptor.

dc.creatorPontes-de-Carvalho, Lain Carlos
dc.creatorTomlinson, Stephen
dc.creatorVandekerckhove, Filip
dc.creatorBienen, E. Jay
dc.creatorClarkson, S Allen B
dc.creatorJiang, Man-Shiow
dc.creatorHart, Gerald W
dc.creatorNussenzweig, Victor
dc.date2014-09-09T18:57:15Z
dc.date2014-09-09T18:57:15Z
dc.date1993
dc.date.accessioned2023-09-26T22:54:29Z
dc.date.available2023-09-26T22:54:29Z
dc.identifierPONTES-DE-CARVALHO, L.C. et al. Characterization of a novel trans-sialidase of Trypanosoma brucei procyclic trypomastigotes and identification of procyclin as the main sialic acid acceptor. Journal of Experimental Medicine, v. 177, n. 2, p. 465-474, 1993.
dc.identifier0022-1007
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/8338
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8884619
dc.descriptionHere we report the presence of a trans-sialidase on the surface of Trypanosoma brucei culturederived procyclic trypomastigotes. The enzyme is not detected in lysates of bloodstream trypomastigotes enriched for either stumpy or slender forms. The trans-sialidase catalyzes the transfer of ot(2-3)-linked sialic acid residues to lactose./3-galactopyranosyl residues are at least 100 times better acceptors for sialic acid than ot-galactopyranosyl residues. In the absence of efficient acceptors, the purified enzyme transfers sialic acid to water, i.e., it acts as a sialidase. Although the T. cruzi and T. brucei trans-sialidases have very similar donor and acceptor specificities, they are antigenicaUy distinct. Sodium dodecyl sulfate--polyacramide gel electrophoresis under nonreducing conditions and silver staining of the purified trans-sialidase reveals a single band of 63 kD. When the surface membrane of live procyclic trypomastigotes is trans-sialylated, using radioactive sialyllactose as the donor substrate, it appears that the only sialylated surface molecule is procyclin. Pronase treatment of live parasites removes only part of the surface sialic acid, in agreement with recent data showing that the glycosylphosphatidylinositol anchor of procyclin is sialylated (Ferguson, M. A. J., M. Murray, H. Rutherford, and M. J. McConville. 1993. Biochem. J. In press).
dc.formatapplication/pdf
dc.languageeng
dc.publisherThe Rockefeller University Press
dc.rightsopen access
dc.subjectGlicoproteínas de Membrana
dc.subjectSialiltransferases/metabolismo
dc.subjectTrypanosoma brucei brucei/enzimologia
dc.subjectGlicoproteínas Variantes de Superfície de Trypanosoma/metabolismo
dc.subjectAnimais
dc.subjectNeuraminidase/metabolismo
dc.subjectProteínas de Protozoários/isolamento & purificação
dc.subjectProteínas de Protozoários/metabolismo
dc.subjectÁcidos Siálicos/metabolismo
dc.subjectSialoglicoproteínas/metabolismo
dc.subjectSialiltransferases/isolamento & purificação
dc.subjectTrypanosoma brucei brucei/citologia
dc.subjectTrypanosoma cruzi/enzimologia
dc.titleCharacterization of a novel trans-sialidase of Trypanosoma brucei procyclic trypomastigotes and identification of procyclin as the main sialic acid acceptor.
dc.typeArticle


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